Document Detail

Synthesis and degradation of acyl peptide using enzyme from Pseudomonas aeruginosa.
MedLine Citation:
PMID:  18397780     Owner:  NLM     Status:  MEDLINE    
The detailed properties of the enzyme from Pseudomonas aeruginosa, which catalyzes the N-acyl linkage between myristic acid and the N-terminal glycine residue of the octapeptide GNAAAARR-NH(2) (PKA) in aqueous solution without ATP and CoA, were studied. The substrate specificity for the acyl peptide in the synthetic reaction was examined, and it was found that at least eight amino acid residues are required for the reaction and that the N-terminal glycine residue is not absolutely essential for the reaction because the activity was detected using the octapeptide that has an N-terminal alanine. The activity was also strongly affected by the amino acid sequence because the activity was very weak in the reaction using GARASVLS-NH(2) (HIV-1p17(gag)). The substrate specificity for fatty acids was also examined. In the reactions using lauric acid and decanoic acid, only slight activities were detected; however, those activities were very small compared with the activity in the reaction using myristic acid. In addition, the degradation of myristoyl PKA by the enzyme was detected, although there are only a few reports on demyristoylation. The optimum pH and temperature of the degradation reaction were consistent with those of the synthetic reaction. The degradation reaction was inhibited by divalent cations.
Nazneen Naher Islam; Koichi Igarashi; Taro Tachibana; Hiroshi Ooshima; Masayuki Azuma
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of bioscience and bioengineering     Volume:  105     ISSN:  1389-1723     ISO Abbreviation:  J. Biosci. Bioeng.     Publication Date:  2008 Mar 
Date Detail:
Created Date:  2008-04-09     Completed Date:  2008-08-19     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100888800     Medline TA:  J Biosci Bioeng     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  282-7     Citation Subset:  IM    
Department of Applied Chemistry and Bioengineering, Graduate School of Engineering, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan.
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MeSH Terms
Acyl Coenzyme A / chemistry
Adenosine Triphosphate / chemistry
Cyclic AMP-Dependent Protein Kinases / chemistry
Glycine / chemistry
Mass Spectrometry
Myristic Acids / chemistry*
Oligopeptides / chemistry*
Pseudomonas aeruginosa / enzymology*
Substrate Specificity
Reg. No./Substance:
0/Acyl Coenzyme A; 0/Myristic Acids; 0/Oligopeptides; 56-40-6/Glycine; 56-65-5/Adenosine Triphosphate; EC AMP-Dependent Protein Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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